Structure of the complex formed by human interleukin-2 and scFv F10. Determined by X-ray diffraction at 1.71 Å resolution. Released 4 Sept 2024.
Explore 8SOW in 3D Show helices and sheets RCSB PDB PDBe
8SOW contains 13 α-helices and 27 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-29 | 23 | |
| α-helix | 36-39 | 4 | |
| β-strand | 44 | 1 | 6 |
| β-strand | 47 | 1 | 7 |
| α-helix | 53-56 | 4 | |
| α-helix | 57-60 | 4 | |
| α-helix | 63-70 | 8 | |
| α-helix | 83-97 | 15 | |
| β-strand | 107 | 1 | 7 |
| β-strand | 112 | 1 | 6 |
| α-helix | 114-129 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 11-12 | 2 | 2 |
| β-strand | 18-25 | 8 | 1 |
| β-strand | 34-39 | 6 | 3 |
| β-strand | 46-51 | 6 | 3 |
| β-strand | 57-59 | 3 | 3 |
| β-strand | 67-72 | 6 | 1 |
| β-strand | 77-82 | 6 | 1 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-97 | 7 | 3 |
| β-strand | 103-104 | 2 | 3 |
| β-strand | 108-110 | 3 | 3 |
| β-strand | 111-112 | 2 | 2 |
| β-strand | 138-141 | 4 | 4 |
| β-strand | 144-146 | 3 | 5 |
| β-strand | 153-159 | 7 | 4 |
| β-strand | 167-172 | 6 | 5 |
| α-helix | 177-178 | 2 | |
| β-strand | 179-183 | 5 | 5 |
| β-strand | 187-188 | 2 | 5 |
| α-helix | 189 | 1 | |
| β-strand | 196-200 | 5 | 4 |
| β-strand | 204-209 | 6 | 4 |
| α-helix | 214-216 | 3 | |
| β-strand | 218-224 | 7 | 5 |
| α-helix | 231 | 1 | |
| β-strand | 232 | 1 | 5 |
| α-helix | 233 | 1 | |
| β-strand | 236-239 | 4 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| F10 single chain fragment variable | C | protein | 241 | Homo sapiens | |
| Interleukin-2 | A | protein | 139 | Homo sapiens | P60568 (AlphaFold model) |
>8SOW_1 F10 single chain fragment variable (chains C) EVQLQESGPGLVAPSQSLSITCTVSGFSLTNYDISWIRQPPGKGLEWLGVIWTGGGTNYN SGFMSRLSITKDNSKSQVFLKMNSLQTDDTAIYYCVRQGRSPYWGQGTLVTVSAGILGSG GGGSGGGGSGGGGSDIQVTQSPSSLSVSLGDRVTITCKASKDIYNRLAWYQQKPGNAPRL LISGATSLETGVPSRFSGSGSGKDYTLTITSLQTEDVATYYCQQSWDTPYTFGGGTKLEI K
>8SOW_2 Interleukin-2 (chains A) AGSAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQ CLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEF LNRWITFCQSIISTLTAAA
Engineered cytokine/antibody fusion proteins improve IL-2 delivery to pro-inflammatory cells and promote antitumor activity. Leonard, E.K., Tomala, J., Gould, J.R. et al. JCI Insight (2024) 9. DOI 10.1172/jci.insight.173469 · PubMed
Other PDB entries of the same protein (UniProt P60568 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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